Evidence map›Paper›PMID 11752309›Full record

ArticleNucleic acids research2002

MODBASE, a database of annotated comparative protein structure models.

Ursula Pieper, Narayanan Eswar, Ashley C Stuart, Valentin A Ilyin, Andrej Sali

Abstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed.

  1. Article
  2. VInternational journal of molecular sciences · 2022
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Biodegradation of single-walled carbon nanotubes by eosinophil peroxidase.Small (Weinheim an der Bergstrasse, Germany) · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. Function of human Rh based on structure of RhCG at 2.1 A.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. Article
  16. Article
  17. Article
  18. Advances in homology protein structure modeling.Current protein & peptide science · 2006
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Ursula PieperLaboratories of Molecular Biophysics, The Pels Family Center for Biochemistry and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Narayanan Eswar
Ashley C Stuart
Valentin A Ilyin
Andrej Sali

Funding

CENTER FOR STRUCTURAL GENOMICSP50GM062529 · NIGMS · SGX PHARMACEUTICALS, INC. · PI BURLEY, STEPHEN KEVIN · 2000 to 2004
$33.8M
Protein Modeling by Satisfaction of Spatial RestraintsR01GM054762 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2001 to 2008
$2.1M
NIGMS NIH HHS GM P50 6M62529NIGMS NIH HHS GM R01 54762
6 · The paper itself

Abstract

MODBASE (http://guitar.rockefeller.edu/modbase) is a relational database of annotated comparative protein structure models for all available protein sequences matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on PSI-BLAST, IMPALA and MODELLER. MODBASE uses the MySQL relational database management system for flexible and efficient querying, and the MODVIEW Netscape plugin for viewing and manipulating multiple sequences and structures. It is updated regularly to reflect the growth of the protein sequence and structure databases, as well as improvements in the software for calculating the models. For ease of access, MODBASE is organized into different datasets. The largest dataset contains models for domains in 304 517 out of 539 171 unique protein sequences in the complete TrEMBL database (23 March 2001); only models based on significant alignments (PSI-BLAST E-value < 10(-4)) and models assessed to have the correct fold are included. Other datasets include models for target selection and structure-based annotation by the New York Structural Genomics Research Consortium, models for prediction of genes in the Drosophila melanogaster genome, models for structure determination of several ribosomal particles and models calculated by the MODWEB comparative modeling web server.

Indexed as

Databases, ProteinModels, MolecularAnimalsComputer GraphicsDatabase Management SystemsDrosophila melanogasterForecastingGenomeHumansInformation Storage and RetrievalInternetProteinsProtein Structure, TertiaryRibosomal ProteinsSequence AlignmentSequence Homology, Amino AcidProteinsRibosomal Proteins

Identifiers

PMID11752309
PMCPMC99112

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.